2R9P: Human mesotrypsin

Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor(BPTI). Determined by X-ray diffraction at 1.4 Å resolution. Released 11 Dec 2007.

Method: X-ray diffraction
Resolution: 1.4 Å
Organisms: Homo sapiens, Bos taurus
Chains: 8
Atoms: 9,414
Mol. weight: 125.06 kDa
Released: 11 Dec 2007

Explore 2R9P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2R9P contains 46 α-helices and 96 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-34	5	3
β-strand	40-46	7	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	64-67	4	3
β-strand	72	1	4
β-strand	81-90	10	3
β-strand	104-108	5	3
α-helix	111-114	4
β-strand	115	1	5
β-strand	118	1	5
β-strand	122	1	2
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	2
β-strand	154	1	4
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-201	4	2
β-strand	204-215	8	2
β-strand	221A	1	6
β-strand	224	1	6
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-243	9

Chain B: 8 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	7
β-strand	20-21	2	8
α-helix	22-23	2
β-strand	30-37	6	9
β-strand	39-48	10	9
β-strand	51-54	4	9
α-helix	56-58	3
β-strand	64-67	4	9
β-strand	72	1	10
β-strand	81-90	10	9
β-strand	104-108	5	9
β-strand	122	1	8
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	8
β-strand	154	1	10
β-strand	156-162	7	8
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	8
β-strand	189	1	7
β-strand	198-201	4	8
β-strand	204-215	8	8
β-strand	226-230	5	8
α-helix	231-234	4
α-helix	235-245	11

Chain C: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	11
β-strand	20-21	2	12
α-helix	22-23	2
α-helix	24-26	3
β-strand	30-34	5	13
β-strand	40-46	7	13
β-strand	51-54	4	13
α-helix	56-58	3
β-strand	64-67	4	13
β-strand	72	1	14
β-strand	81-90	10	13
β-strand	104-108	5	13
α-helix	111-114	4
α-helix	120-121	2
β-strand	122	1	12
α-helix	123-124	2
β-strand	135-140	6	12
β-strand	154	1	14
β-strand	156-162	7	12
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	12
β-strand	189	1	11
β-strand	198-201	4	12
β-strand	204-215	8	12
β-strand	221A	1	15
β-strand	224	1	15
β-strand	226-230	5	12
α-helix	231-234	4
α-helix	235-243	9

Chain D: 8 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	16
β-strand	20-21	2	17
α-helix	22-23	2
β-strand	30-34	5	18
β-strand	40-48	9	18
β-strand	51-54	4	18
α-helix	56-58	3
β-strand	64-67	4	18
β-strand	72	1	19
β-strand	81-90	10	18
β-strand	104-108	5	18
α-helix	111-114	4
β-strand	122	1	17
α-helix	123-124	2
β-strand	135-140	6	17
β-strand	146	1	20
β-strand	148	1	20
β-strand	154	1	19
β-strand	156-162	7	17
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	17
β-strand	189	1	16
β-strand	198-201	4	17
β-strand	204-215	8	17
β-strand	226-230	5	17
α-helix	231-234	4
α-helix	235-245	11

Chains E, F and I: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4
α-helix	8-9	2
β-strand	14	1	2
β-strand	18-24	7	22
β-strand	29-35	7	22
β-strand	45	1	22
α-helix	48-55	8

Chain G: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-9	2
β-strand	14	1	12
β-strand	18-24	7	24
β-strand	29-35	7	24
β-strand	45	1	24
α-helix	48-55	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Trypsin-3	A, B, C, D	protein	224	Homo sapiens	P35030 (AlphaFold model)
Pancreatic trypsin inhibitor	E, F, G, I	protein	58	Bos taurus	P00974 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2R9P_1 Trypsin-3 (chains A, B, C, D)
IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEG
NEQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG
WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSMFCVGFLEGGKDSCQRDAGGP
VVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS

Sequence of entity 2 (E, F, G, I), FASTA

>2R9P_2 Pancreatic trypsin inhibitor (chains E, F, G, I)
RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA

Primary citation

Structural Basis for Accelerated Cleavage of Bovine Pancreatic Trypsin Inhibitor (BPTI) by Human Mesotrypsin. Salameh, M.A., Soares, A.S., Hockla, A. et al. J Biol Chem (2008) 283:4115-4123. DOI 10.1074/jbc.M708268200 · PubMed

Other PDB entries of the same protein (UniProt P35030 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5TP0 1.25 Å, Human mesotrypsin in complex with diminazene
3P95 1.3 Å, Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant…
4DG4 1.4 Å, Human mesotrypsin-S39Y complexed with bovine pancreatic trypsin inhibitor (BPTI)
5JBT 1.4 Å, Mesotrypsin in complex with cleaved amyloid precursor like protein 2 inhibitor (APLP2)
3P92 1.6 Å, Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant…
9BOT 1.6 Å, Human mesotrypsin (PRSS3) unliganded and in autoinhibited (E*) conformation
4U32 1.65 Å, Human mesotrypsin complexed with HAI-2 Kunitz domain 1
1H4W 1.7 Å, Structure of human trypsin IV (brain trypsin)
9BOS 1.7 Å, Human mesotrypsin (PRSS3) unliganded and in an active (E) conformation
5C67 1.83 Å, Human Mesotrypsin in complex with amyloid precursor protein inhibitor variant…
6BX8 1.98 Å, Human Mesotrypsin (PRSS3) Complexed with Tissue Factor Pathway Inhibitor Variant…
6GFI 2.3 Å, Structure of Human Mesotrypsin in complex with APPI variant T11V/M17R/I18F/F34V

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